CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.
Difference between revisions of "Carbohydrate Binding Module Family 92"
Xuanwei Mei (talk | contribs) |
Xuanwei Mei (talk | contribs) |
||
Line 25: | Line 25: | ||
== Functionalities == | == Functionalities == | ||
− | + | ||
In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>. | In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A <cite>Shen2018</cite> (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the ''in situ'' investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The ''in situ'' visualization of carrageenan in red alga ''Kappaphycus alvarezii'' was realized by utilizing the fluorescent probe <cite>Mei2022</cite>. |
Revision as of 23:00, 12 April 2023
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
CAZy DB link | |
http://www.cazy.org/CBM92.html |
Ligand specificities
The first characterized member in the CBM92 family is from Cgk16A-CBM92 from the marine bacterium Wenyingzhuangia aestuarii OF219 [1]. The CBM92 bound specifically to carrageenan. It was incapable of binding to other polysaccharide components in red algae including agarose, porphyran, and funoran [1]. Meanwhile, the CBM92 displayed no affinity to several anionic polysaccharides, namely pectin, chondroitin sulfates, dermatan sulfate, and sulfated fucans [1]. The CBM92 showed no significant difference in the affinity to κ- and ι-carrageenan.
Structural Features
No three-dimensional structure has been solved in this CBM family at present. Several conserved residues (e.g., Phe-70, Arg-72, and Phe-75) were discovered through the multiple sequence alignments of Cgk16A-CBM92 and its close homologs [1], which might be critical for the ligand binding of this CBM.
Functionalities
In the natural context, Cgk16A-CBM92 is a component of the κ-carrageenase Cgk16A [2] (Fig. 1). It thus might maintain the enzyme near its substrate to improve the enzymatic activity via the proximity effect. To evaluate the feasibility of Cgk16A-CBM92 as a tool in the in situ investigation of carrageenan, a fluorescent probe was constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The in situ visualization of carrageenan in red alga Kappaphycus alvarezii was realized by utilizing the fluorescent probe [1].
Members of the CBM92 family are present in different glycoside hydrolase (GH) family sequences, e.g., GH16_17, GH5_54, GH19, and GH95. According to the CAZy database, these GH families comprise enzymes with various substrate specificities, including κ-carrageenase (GH16_17), chitinase (GH19), fucosidase (GH95), and galactosidase (GH95). It indicated that functional diversity might be present within the CBM92 family.
Family Firsts
- First Identified
- The first characterized CBM92 member [1] is a component of the κ-carrageenase Cgk16A [2], which was discovered from a marine bacterium Wenyingzhuangia aestuarii OF219.
- First Structural Characterization
- No three-dimensional structure has been solved in this CBM family at present.
References
- Mei X, Chang Y, Shen J, Zhang Y, Han J, and Xue C. (2022). Characterization of a Novel Carrageenan-Specific Carbohydrate-Binding Module: a Promising Tool for the In Situ Investigation of Carrageenan. J Agric Food Chem. 2022;70(29):9066-9072. DOI:10.1021/acs.jafc.2c03139 |
- Shen J, Chang Y, Chen F, and Dong S. (2018). Expression and characterization of a κ-carrageenase from marine bacterium Wenyingzhuangia aestuarii OF219: A biotechnological tool for the depolymerization of κ-carrageenan. Int J Biol Macromol. 2018;112:93-100. DOI:10.1016/j.ijbiomac.2018.01.075 |